SEED STORAGE PROTEINS

PRESENTED BY:
DIVYA KAUSHIK
M.Sc BIOTECHNOLOGY
2nd SEMESTER
 INTRODUCTION
 The plant seed is not only an organ of propagation and dispersal
but also the major plant tissue harvested by humankind.
 The amount of protein present in seeds varies from 10% (in
cereals) to 40% (in certain legumes and oilseeds) of the dry
weight, forming a major source of dietary protein.
 Although the vast majority of the individual proteins present in
mature seeds have either metabolic or structural roles, all seeds
also contain one or more groups of proteins that are present in
high amounts and that serve to provide a store of amino acids
for use during germination and seedling growth.
 These storage proteins are of particular importance because
they determine not only the total protein content of the seed
but also its quality for various end uses.
 CHARACTERISTICS OF SEED STORAGE
PROTEINS

 Seed storage proteins (SSPs) are specifically synthesized

during seed maturation and accumulate in the endosperm of
monocots or in the cotyledons and embryos of dicots.
 Their presence in mature seeds in discrete deposit are called
protein bodies. One of the earliest and first isolated
proteins is wheat gluten and Brazil nut globulin.
 They are synthesized at high levels in specific tissues and at
certain stages of development.
 their synthesis is regulated by nutrition, and they act as a
sink for surplus nitrogen.
 CLASSIFICATION
Classification of proteins in to their groups is
based on their solubility. Three protein groups
have been categorized during classification
(Osborne’s classical definitions).

Albumin • Water soluble

Globulin • Dilute salt soluble

• Alcohol/water micture
Prolamins soluble
• Dilute acid or alkali
Glutelins •
 CLASSIFICATION OF PROTEINS BASED ON
THEIR SOLUBILITY

2S GLOBULIN PROLAMIN
ALBUMIN • 11S globulin • Gliadin (S-rich)
• napin • C hordein (S-
• 7S globulin poor)
• Conglotin
• HMW subunit
• Sunflower • Avenin
SFAS • Zein
• Castor bean • Rice S-rich
albumin prolamin
 2S ALBUMIN STORAGE PROTEINS

 The 2s albumins were initially defined as a group on

the basis of their sedimentation coefficients (S20.w).
 They are widely distributed in dicot seeds and have
been most widely studied in the Cruciferae, notably
oilseed rape (in which they are called napins) and
Arabidopsis.
 They are synthesized as single precursor proteins that
are proteolytically cleaved with the loss of a linker
peptide and short peptides from both the N and C
termini.
 GLOBULINS

 Present in embryo and outer aleurone layer of

the endosperm.
 Readily soluble in dilute salt solution.

 Sedimentation coefficient is about 7.

 Usually removed by milling (wheat), polishing

(rice), pearling (barley) or decortication
(sorghum), before human consumption.
 Storage globulins of 11S located in the starchy
endosperm are also present in atleast some
cereal grains.
HYPOTHETIC PATHWAY FOR THE EVOLUTION OF
GERMINS AND GLOBULIN STORAGE PROTEINS
 PROLAMINS

 Major endosperm storage proteins of all cereal grains

(except rice and oat).
 Generally rich in proline and amide nitrogen derived
from glutamine.
 Soluble in alcohol/water mixtures (eg. 60-70% (v/v)
ethanol).
 Much more variable in structure than the 7S and 11S
globulins.
 Present in wheat, barley, rye, maize, sorghum,
millets.
 Presence of amino acid sequences consisting of
repeated blocks based on one or more short peptide
motifs (eg. Methionine, glycine, histidine etc) eg. Zein.
 GLUTELINS

 Glutelins soluble in dilute acids or bases.

 They are generally prolamin like proteins in
certain grass seeds eg. Wheat.
 Glutenin is the most common glutelin found in
wheat.
 It imparts baking quality to wheat.

 it is known that glutelin, a major storage protein

in rice, originates from the same ancestral gene
as leguminous 11S globulin irrespective of
difference in solubility.
GLUTELIN STRUCTURE
DECOMPOSITION OF SSPS AT SEED GERMINATION STAGE
 SSPs provide material for new protein synthesis, and nitrogen
source and sulfur source during germination.
 SSP decomposition has been predominantly studied in seeds
of cultivated plants such as cereal grains and legumes.
 SSPs are broken down into soluble peptides by endopeptidase,
and subsequently these peptides are decomposed into smaller
peptides or amino acids by exopeptidase.
 Peptidase is secreted from the cotyledons in dicots and from
the aleurone layer and scutellum in monocots after water
absorption by the seed.
 This peptidase secretion is triggered by the plant hormone
gibberellin (GA).
 Amino acids produced from decomposition of SSPs are used as
a source for new protein synthesis during germination and
subsequent seedling growth.
 ENGINEERING PLANT SEED STORAGE PROTEINS
 Present strategy in the modification of seed storage
protein is mainly focused on increasing concentration
of sulphur containing amino acids (S-rich amino
acids) in legume seeds and lysine content in cereals.
 Since animal system (including human) cannot
synthesize certain essential amino acids, dietary
supply can overcome this problem. Cereal grains
containing lysine rich protein consumed as high
profile energy source in the diet of humans and lives
stock.
 Cereal seeds however, generally tend to be deficient
in lysine, threonine and tryptophan.
 In contrast, legumes seed is the richest source for
proteins (upto 40%) but shows, deficient in
methionine and cysteine content as well as
tryptophan (sulphur containing amino acid) for
example, pea seed protein containing around 0.8%
methionine and 1.0% cysteine. This level is
insufficient for growth and development.
 Lives stock animals however, require 3.5% by weight
of dietery protein. Besides, people who consumes
only vegetarian food suffers health problem due to
amino acid imbalance. Therefore, breeding and
genetic engineering methods can drive increase in
concentration of essential amino acid to overcome
nutritional imbalance.
TRANSGENIC TECHNOLOGY FOR TAILORING
THE QUALITY OF SEED STORAGE PROTEIN
 Transgenic technology for tailoring the
quality of seed storage protein
Transgenic
Gene Promoter plant
Improvement

2S rich zein
CAM V35S Alfa alfa S content
(maize)

2S protein (brazil Vicia

CAM V35S methionine
nut) narborensis

2S protein Sulphur
CAM V35S Legumes
(sunflower) content

Beta phaseolin Rice glu

rice lysine
(common bean) promoter
Ferritin Rice glu B1
Rice Fe content
(soyabean) promoter
 NOVEL APPLICATION OF SSPS
 Seeds, especially crop seeds, have attracted attention as a
production platform for valuable proteins or peptides.
 Transgenic seed has many advantages as a bioreactor,
because high-level expression of recombinant protein can be
easily achieved.
 Engineered peptides can be produced and sequestered
exclusively in the seed without causing deleterious effects in
other vegetative tissues, when specifically expressed in seed.
 Furthermore, recombinant proteins are stable in transgenic
seed for several years at room temperature.
 It is possible that transgenic seeds could easily provide
bioactive function by oral feeding without extraction of
bioactive components.
 APPLICATIONS CONTD..
 SSPs are useful for high accumulation of recombinant
protein as carrier protein.
 SSP-fused recombinant protein can be easily deposited
in seed cells.
 SSP-fused recombinant protein (peptide) expressed
under the control of the SSP promoter provides an ideal
combination as an accumulation system for
recombinant protein.
 Soybean glycinin, rice glutelin, and their promoters are
actually used for accumulation of bioactive peptides or
epitopic peptides.
 Transgenic seed accumulating human health promoting
proteins may be practically used as bioactive foods in
the future.
REFERENCES
 http://www.biologydiscussion.com/plants/plants-
with-improved-quality-of-nutrition/72129
 http://www.plantcell.org/content/plantcell/7/7/945
.full.pdf
 H.B. Krishnan, E.H. CoeJr (2001), Seed Storage
Proteins, Encyclopedia of Genetics.
 P.R. Shewry (2004), Protein Chemistry Of
Dicotyledonous Grains, Encyclopedia of Grain
Science.